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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Heart Rhythm. 2011 Jan 11;8(6):938–941. doi: 10.1016/j.hrthm.2011.01.018

Figure 2. Putative CaMKII phosphorylation sites in Kv4.3, Kvβ2, and KChIP2.

Figure 2

(A) The T1 domain of one Kv4.3 α subunit associated with Kvβ2 and KChIP2 accessory subunits. Putative CaMKII phosphorylation sites are shown in orange for Kv4.3 (residue T53) and green for Kvβ2 (residues S112, S132, T174, and S192). (B) Linear sequences of the hKv4.3C terminus and the hKChIP2N terminus with additional putative CaMKII phosphorylation sites in red